New methods for protein structure determination are being applied to membrane proteins. These proteins represent 30% of the proteins encoded by the human genome. Therefore a method to solve the structures of this important class of proteins will provide insight into their biological functions. The complete resolution of the spectral parameters of the fd and pf1 viral coat proteins in lipid bilayers was accomplished using solid-state NMR. The method of structure determination by solid-state NMR requires that the spectral parameters for analysis be resolved and assigned. The methods of two and three-dimensional NMR spectroscopy applied to the spin interactions present in immobilized proteins are demonstrated on these two proteins to further the development of the structure method. 15N chemical shift anisotropy (CSA), 1H CSA and 15N-1H dipolar couplings were measured for all of the sites in the fd coat protein. The tabulation of these orientation dependent spin interactions provides the data set for the structure determination by solid-state NMR.